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Molecule Parameter List for CaMKII-CaM

The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network.
The text color of a molecule is highlighted by color.
Statistics
CaMKII-CaM participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1102101

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Osc_Ca_
    IP3metabolism
  • 32Network
    MIPP CaMKII CaM 
    PKC IP3-3K Gq 
    PLCbeta 134_dephos 145_dephos 
    IP4-system IHP-system 1345_dephos 
    CaRegulation Othmer-Tang-model 
    This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316.

    CaMKII-CaM acting as a Molecule in  
    Osc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    CaMKII-CaM
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    01000No
    This is the regular, CaM-activated form of CaMKII. See the review Hanson and Schulman 1992 Ann. Rev. Biochem 60:559-601

    CaMKII-CaM acting as a Summed Molecule in  
    Osc_Ca_IP3metabolism Network
    Accession NamePathway NameTargetInput
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    tot_CaM_CaMKIICaMKII-CaM
  • CaMKII-thr286*-C
    aM

  • This pool sums the levels of the CaM-bound forms of CaMKII: CaMKII-CaM + CaMKII-thr286*-CaM. Although their phosphorylation states are different, the level of activity is about the same so it makes sense to sum the levels. Hanson et al 1994 Neuron 12:943-956

    CaMKII-CaM acting as a Substrate for an Enzyme in  
    Osc_Ca_IP3metabolism Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1tot_CaM_CaMKII  /
    CaM_act_286
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    0.000002705630.54explicit E-S complexSubstrate
    CaMKII-CaM

    Product
  • CaMKII-thr286*-C
    aM

  •     See Hanson and Schulman 1992 JBC 267(24):17216-17224
    2
  • tot_autonomous_
    CaMKII
      /
    auton_286
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    0.000004166670.54explicit E-S complexSubstrate
    CaMKII-CaM

    Product
  • CaMKII-thr286*-C
    aM

  •     The autonomous rate has a slightly higher Km than the CaM-bound rate, but Vmax is the same. Hanson and Schulman 1992 Ann Rev Biochem 61:559-601 and Hanson and Schulman 1992 JBC 267(24):17216-17224

    CaMKII-CaM acting as a Product of an Enzyme in  
    Osc_Ca_IP3metabolism Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PP1-active  /
    Deph-thr286
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    5.099070.354explicit E-S complexSubstrate
  • CaMKII-thr286*-C
    aM


    Product
    CaMKII-CaM
  • The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.

    CaMKII-CaM acting as a Product in a reaction in  
    Osc_Ca_IP3metabolism Network
    Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reaction are not consider.
    NameAccession NamePathway NameKfKbKdtauReagents
    CaMKII-bind-CaM
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    49.9998
    (uM^-1 s^-1)
    5
    (s^-1)
    Kd(bf) = 0.1(uM)-Substrate
    CaM-Ca4
    CaMKII

    Product
    CaMKII-CaM
    This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol.



    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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